Multi-scale Approaches to Dynamical Transmission of Protein Allostery (2015)
Conference Proceeding
Townsend, P., Rodgers, T., Pohl, E., Wilson, M., Cann, M., & McLeish, T. (2015). Multi-scale Approaches to Dynamical Transmission of Protein Allostery. In L. Olivares-Quiroz, O. Guzmán-López, & H. E. Jardón-Valadez (Eds.), Physical Biology of Proteins and Peptides: Theory, Experiment, and Simulation (141-152). https://doi.org/10.1007/978-3-319-21687-4_8

We review the idea that allosteric interactions can be transmitted not by structural switching but by the more subtle route of modulation of the amplitude of thermally-activated global dynamical modes in allosteric proteins. The effect is naturally a... Read More about Multi-scale Approaches to Dynamical Transmission of Protein Allostery.

Are there ergodic limits to evolution? Ergodic exploration of genome space and convergence (2015)
Journal Article
McLeish, T. (2015). Are there ergodic limits to evolution? Ergodic exploration of genome space and convergence. Interface Focus, 5(6), Article 20150041. https://doi.org/10.1098/rsfs.2015.0041

We examine the analogy between evolutionary dynamics and statistical mechanics to include the fundamental question of ergodicity—the representative exploration of the space of possible states (in the case of evolution this is genome space). Several p... Read More about Are there ergodic limits to evolution? Ergodic exploration of genome space and convergence.

Dynamic Transmission of Protein Allostery without Structural Change: Spatial Pathways or Global Modes? (2015)
Journal Article
McLeish, T., Cann, M., & Rodgers, T. (2015). Dynamic Transmission of Protein Allostery without Structural Change: Spatial Pathways or Global Modes?. Biophysical Journal, 109(6), 1240-1250. https://doi.org/10.1016/j.bpj.2015.08.009

We examine the contrast between mechanisms for allosteric signaling that involve structural change, and those that do not, from the perspective of allosteric pathways. In particular we treat in detail the case of fluctuation-allostery by which amplit... Read More about Dynamic Transmission of Protein Allostery without Structural Change: Spatial Pathways or Global Modes?.

The role of protein-ligand contacts in allosteric regulation of the Escherichia coli Catabolite Activator Protein (2015)
Journal Article
Townsend, P., Rodgers, T., Glover, L., Korhonen, H., Richards, S., Colwell, L., …Cann, M. (2015). The role of protein-ligand contacts in allosteric regulation of the Escherichia coli Catabolite Activator Protein. Journal of Biological Chemistry, 290(36), 22225-22235. https://doi.org/10.1074/jbc.m115.669267

Allostery is a fundamental process by which ligand binding to a protein alters its activity at a distant site. Both experimental and theoretical evidence demonstrate that allostery can be communicated through altered slow relaxation protein dynamics... Read More about The role of protein-ligand contacts in allosteric regulation of the Escherichia coli Catabolite Activator Protein.

The search for affirming narratives for the future governance of thechnology : reflections from a science-theology persective on GMFuturos (2015)
Book Chapter
McLeish, T. (2016). The search for affirming narratives for the future governance of thechnology : reflections from a science-theology persective on GMFuturos. In P. Macnaghten, & S. Carro-Ripalda (Eds.), Governing agricultural sustainability : global lessons from GM crops (192-197). Routledge

Global low-frequency motions in protein allostery: CAP as a model system (2015)
Journal Article
Townsend, P., Rogers, T., Pohl, E., Wilson, M., McLeish, T., & Cann, M. (2015). Global low-frequency motions in protein allostery: CAP as a model system. Biophysical Reviews, 7(2), 175-182. https://doi.org/10.1007/s12551-015-0163-9

Allostery is a fundamental process by which ligand binding to a protein alters its activity at a distant site. There is considerable evidence that allosteric cooperativity can be communicated by the modulation of protein dynamics without conformation... Read More about Global low-frequency motions in protein allostery: CAP as a model system.